8xvc

CryoEM structure of ADP-DNA-MuB conformation1

Method: ELECTRON MICROSCOPY

1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP-dependent target DNA activator B

Escherichia phage Mu

UniProt P03763

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 18 ADENOSINE-5'-DIPHOSPHATE × 18 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TARGB_BPMU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–312; UniProt 1–312 Author chain B; PDBConstruct 1–312; UniProt 1–312 Author chain C; PDBConstruct 1–312; UniProt 1–312 Author chain D; PDBConstruct 1–312; UniProt 1–312 Author chain E; PDBConstruct 1–312; UniProt 1–312 Author chain F; PDBConstruct 1–312; UniProt 1–312 Author chain G; PDBConstruct 1–312; UniProt 1–312 Author chain H; PDBConstruct 1–312; UniProt 1–312 Author chain I; PDBConstruct 1–312; UniProt 1–312 Author chain J; PDBConstruct 1–312; UniProt 1–312 Author chain K; PDBConstruct 1–312; UniProt 1–312 Author chain L; PDBConstruct 1–312; UniProt 1–312 Author chain M; PDBConstruct 1–312; UniProt 1–312 Author chain N; PDBConstruct 1–312; UniProt 1–312 Author chain O; PDBConstruct 1–312; UniProt 1–312 Author chain P; PDBConstruct 1–312; UniProt 1–312 Author chain Q; PDBConstruct 1–312; UniProt 1–312 Author chain R; PDBConstruct 1–312; UniProt 1–312

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

2. Structure Basics 2. Structure Basics

Entry ID entry_id8xvc
Deposition date deposition_date2024-01-14
Structure title titleCryoEM structure of ADP-DNA-MuB conformation1
Keywords keywordsMuB, MuB-ADP, Ring, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8xvc__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8xvc__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8xvc__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)56.50 Å
Rg (electron density)55.93 Å
Total Rg55.98 Å
Atom count33840
Residues4230
Excluded volume600380 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8xvc__assembly_1__model_1 18-meric (18) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (2)

7. Citations (1)